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Database: UniProt
Entry: A0A1G9K9G6_9FLAO
LinkDB: A0A1G9K9G6_9FLAO
Original site: A0A1G9K9G6_9FLAO 
ID   A0A1G9K9G6_9FLAO        Unreviewed;       739 AA.
AC   A0A1G9K9G6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] {ECO:0000256|PIRNR:PIRNR009407};
DE            EC=1.1.1.42 {ECO:0000256|PIRNR:PIRNR009407};
DE   AltName: Full=Oxalosuccinate decarboxylase {ECO:0000256|PIRNR:PIRNR009407};
GN   ORFNames=SAMN04488514_101885 {ECO:0000313|EMBL:SDL45923.1};
OS   Kriegella aquimaris.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Kriegella.
OX   NCBI_TaxID=192904 {ECO:0000313|EMBL:SDL45923.1, ECO:0000313|Proteomes:UP000199440};
RN   [1] {ECO:0000313|EMBL:SDL45923.1, ECO:0000313|Proteomes:UP000199440}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19886 {ECO:0000313|EMBL:SDL45923.1,
RC   ECO:0000313|Proteomes:UP000199440};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH;
CC         Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42;
CC         Evidence={ECO:0000256|PIRNR:PIRNR009407};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR009407-3};
CC       Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.
CC       {ECO:0000256|PIRSR:PIRSR009407-3};
CC   -!- SIMILARITY: Belongs to the monomeric-type IDH family.
CC       {ECO:0000256|PIRNR:PIRNR009407}.
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DR   EMBL; FNGV01000001; SDL45923.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9K9G6; -.
DR   STRING; 192904.SAMN04488514_101885; -.
DR   OrthoDB; 9807643at2; -.
DR   Proteomes; UP000199440; Unassembled WGS sequence.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR004436; Isocitrate_DH_NADP_mono.
DR   NCBIfam; TIGR00178; monomer_idh; 1.
DR   PANTHER; PTHR36999; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR   PANTHER; PTHR36999:SF1; ISOCITRATE DEHYDROGENASE [NADP]; 1.
DR   Pfam; PF03971; IDH; 1.
DR   PIRSF; PIRSF009407; IDH_monmr; 1.
DR   SUPFAM; SSF53659; Isocitrate/Isopropylmalate dehydrogenase-like; 1.
PE   3: Inferred from homology;
KW   Glyoxylate bypass {ECO:0000256|PIRNR:PIRNR009407};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR009407-3};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR009407-3};
KW   NADP {ECO:0000256|PIRNR:PIRNR009407, ECO:0000256|PIRSR:PIRSR009407-4};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR009407};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199440};
KW   Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR009407}.
FT   BINDING         80..85
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         130..137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         133
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         348
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         546
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-2"
FT   BINDING         547
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         551
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-3"
FT   BINDING         583..584
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         588
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         599..601
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   BINDING         648
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-4"
FT   SITE            253
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
FT   SITE            418
FT                   /note="Critical for catalysis"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009407-1"
SQ   SEQUENCE   739 AA;  81043 MW;  B4CA3C7863ABE8B8 CRC64;
     MPKILYTKTD EAPALATQSF LPIVKAFTKT TGIQVETKDI SLAARILAVF PDFLTEDQKV
     SNDLEELGRA AKNPQANIIK LPNISASIPQ LNEVISELQN KGYALPNYPD EPKNDAEKEI
     KSRYDKIKGS AVNPILREGN SDRRAPKAVK NYAKKNPHTM GAWSADSKTH VATMEHGDFK
     ANEKSITLPH ATSIRIELQK TDGTTVVLKE KLALLEGEII DATIMSKKAL LSFLKEQLKD
     AKEKGVLFSL HMKATMMKVS DPIIFGHAVK TFFADVFAKY DTLLASIGAN ANDGLENLLN
     KLKELPEDKR KEIEADIENA IANGPALAMV NSEKGITNLH VPSDVIIDAS MPAMIRNSGK
     MWNAKGELQD TKAVIPDSSY AGIYSATIDF CKKHGAFDPT TMGTVPNVGL MAQKAEEYGS
     HDKTFEIVGD GVVKVIDINS GKTLIEHTVE KGDIWRMCQV KDAPIQDWVK LAVSRARATN
     IPAIFWLDQD RAHDIELTKK VNTYLGDHDI SGLEIKILSP IEATNYTLKR LIKGEDTISV
     SGNVLRDYLT DLFPILEVGT SAKMLSIVPL MNGGGLFETG AGGSAPKHVE QFLEEGHLRW
     DSLGEFMALG VSLEFYGEKN NSPKAQVLAD ALDIATEKLL DNGKSPSRKV NEIDTRGSHF
     YLALYWAQAL AEQNEDAELK SLFTKVSEAL NTNESKIATE LINDQGTPKD IGGYYLPDSD
     LISKAMRPSD TFNGILASI
//
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